Nucleic acid recognition by tandem helical repeats.

Rubinson EH, Eichman BF
Curr Opin Struct Biol. 2012 22 (1): 101-9

PMID: 22154606 · PMCID: PMC3766767 · DOI:10.1016/j.sbi.2011.11.005

Protein domains constructed from tandem α-helical repeats have until recently been primarily associated with protein scaffolds or RNA recognition. Recent crystal structures of human mitochondrial termination factor MTERF1 and Bacillus cereus alkylpurine DNA glycosylase AlkD bound to DNA revealed two new superhelical tandem repeat architectures capable of wrapping around the double helix in unique ways. Unlike DNA sequence recognition motifs that rely mainly on major groove read-out, MTERF and ALK motifs locate target sequences and aberrant nucleotides within DNA by resculpting the double-helix through extensive backbone contacts. Comparisons between MTERF and ALK repeats, together with recent advances in ssRNA recognition by Pumilio/FBF (PUF) domains, provide new insights into the fundamental principles of protein-nucleic acid recognition.

Copyright © 2011 Elsevier Ltd. All rights reserved.

MeSH Terms (6)

Animals DNA Humans Nucleic Acid Conformation Substrate Specificity Tandem Repeat Sequences

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